Collagen Origami

Información del proyecto

Collagen Origami

Identificador del acuerdo de subvención: 891009

DOI

10.3030/891009

Proyecto cerrado

Fecha de la firma de la CE 5 Marzo 2020

Fecha de inicio 1 Septiembre 2020

Fecha de finalización 31 Agosto 2022

Financiado con arreglo a

• EXCELLENT SCIENCE - Marie Skłodowska-Curie Actions

Coste total

€ 203 149,44

Aportación de la UE

€ 203 149,44

Coordinado por

EIDGENOESSISCHE TECHNISCHE HOCHSCHULE ZUERICH
Switzerland

Periodic Reporting for period 1 - Collagen Origami (Collagen Origami)

Período documentado: 2020-09-01 hasta 2022-08-31

Resumen del contexto y de los objetivos generales del proyecto

Collagen is the most abundant protein in mammals and the principal component of connective tissue. Mutations in collagen or its abnormal expression are associated with a number of diseases, e.g. the brittle bone disease or fibrosis. Collagen model peptides (CMPs) which mimic collagen’s intriguing triple-helical structure are used as synthetic surrogates to study this structural protein. In this project, we have shown that the functional groups at the ends of CMPs have a strong impact on the stability of collagen triple helices, a fact that has eluded the scientific community despite the more than 50-year history of CMPs.

Trabajo realizado desde el comienzo del proyecto hasta el final del período abarcado por el informe y los principales resultados hasta la fecha

We have synthesized a series of CMPs with systematically varied terminal functional groups. We used a combined experimental and computational approach to elucidate the origins of the observed effects of the terminal groups on the peptide self-assembly. Our results revealed that the end-groups affect the stability of collagen triple helices by an interplay of two main effects: 1) strand preorganization, i.e. the ability of the individual peptides to pre-form a structure that is suitable for interacting with the other two strands; and 2) interstrand H-bonding, i.e. strengthening the interactions that hold the three strands together. We also show that the contributions of the end-groups are additive and can be used to predict the stability of collagen triple helices.

Avances que van más allá del estado de la técnica e impacto potencial esperado (incluida la repercusión socioeconómica y las implicaciones sociales más amplias del proyecto hasta la fecha)

The ability to rationally design CMPs with predictable properties is an indispensable tool for a multitude of applications. Our findings will guide the design of biological probes and drugs based on collagen hybridizing peptides as well as new synthetic collagen-based materials. Such probes and materials are being currently developed, e.g. as diagnostic tools to monitor tumor boundaries or treatments for chronic wounds. Our results will facilitate the design and implementation of these technologies.

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